Supramolecular multilayer structures of wired redox enzyme electrodes
Supramolecular multilayer structures comprised of glucose oxidase (GOx), and Os complex derivatised poly(allylamine) (PAH-Os) have been built by alternate layer-by-layer (LBL) electrostatic adsorption in a self-assembly process. The resulting modified electrodes with integrated mediator were tested...
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2005
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v7_n8_p1800_Calvo http://hdl.handle.net/20.500.12110/paper_14639076_v7_n8_p1800_Calvo |
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paper:paper_14639076_v7_n8_p1800_Calvo2023-06-08T16:16:37Z Supramolecular multilayer structures of wired redox enzyme electrodes Calvo, Ernesto Julio glucose oxidase polyallylamine polyamine article biocatalysis chemistry electrode genetic procedures kinetics oxidation reduction reaction Biocatalysis Biosensing Techniques Electrodes Glucose Oxidase Kinetics Oxidation-Reduction Polyamines Supramolecular multilayer structures comprised of glucose oxidase (GOx), and Os complex derivatised poly(allylamine) (PAH-Os) have been built by alternate layer-by-layer (LBL) electrostatic adsorption in a self-assembly process. The resulting modified electrodes with integrated mediator were tested as reagentless glucose biosensors. The enzyme kinetic parameters and the surface concentration of "wired" enzyme ΓE have been obtained by analysis of the catalytic current dependence on glucose concentrations for the ping-pong mechanism of glucose oxidation. An average osmium volume concentration was estimated by integration of the redox charge in the absence of glucose and the ellipsometric thickness. The total enzyme surface concentration was measured with a quartz crystal microbalance (QCM) during each adsoption step and the fraction of "wired" enzyme and the bimolecular rate constant for FADH2 oxidation by the redox polymer for the different multilayers. The catalytic current increases with the number of LBL layers because the increase in the enzyme loading while the efficiency of enzyme FADH2 oxidation by the Os redox polymer, except for the first dipping cycle remains almost constant at about 2 × 104 M-1 s-1. © The Owner Societies 2005. Fil:Calvo, E.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2005 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v7_n8_p1800_Calvo http://hdl.handle.net/20.500.12110/paper_14639076_v7_n8_p1800_Calvo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
glucose oxidase polyallylamine polyamine article biocatalysis chemistry electrode genetic procedures kinetics oxidation reduction reaction Biocatalysis Biosensing Techniques Electrodes Glucose Oxidase Kinetics Oxidation-Reduction Polyamines |
| spellingShingle |
glucose oxidase polyallylamine polyamine article biocatalysis chemistry electrode genetic procedures kinetics oxidation reduction reaction Biocatalysis Biosensing Techniques Electrodes Glucose Oxidase Kinetics Oxidation-Reduction Polyamines Calvo, Ernesto Julio Supramolecular multilayer structures of wired redox enzyme electrodes |
| topic_facet |
glucose oxidase polyallylamine polyamine article biocatalysis chemistry electrode genetic procedures kinetics oxidation reduction reaction Biocatalysis Biosensing Techniques Electrodes Glucose Oxidase Kinetics Oxidation-Reduction Polyamines |
| description |
Supramolecular multilayer structures comprised of glucose oxidase (GOx), and Os complex derivatised poly(allylamine) (PAH-Os) have been built by alternate layer-by-layer (LBL) electrostatic adsorption in a self-assembly process. The resulting modified electrodes with integrated mediator were tested as reagentless glucose biosensors. The enzyme kinetic parameters and the surface concentration of "wired" enzyme ΓE have been obtained by analysis of the catalytic current dependence on glucose concentrations for the ping-pong mechanism of glucose oxidation. An average osmium volume concentration was estimated by integration of the redox charge in the absence of glucose and the ellipsometric thickness. The total enzyme surface concentration was measured with a quartz crystal microbalance (QCM) during each adsoption step and the fraction of "wired" enzyme and the bimolecular rate constant for FADH2 oxidation by the redox polymer for the different multilayers. The catalytic current increases with the number of LBL layers because the increase in the enzyme loading while the efficiency of enzyme FADH2 oxidation by the Os redox polymer, except for the first dipping cycle remains almost constant at about 2 × 104 M-1 s-1. © The Owner Societies 2005. |
| author |
Calvo, Ernesto Julio |
| author_facet |
Calvo, Ernesto Julio |
| author_sort |
Calvo, Ernesto Julio |
| title |
Supramolecular multilayer structures of wired redox enzyme electrodes |
| title_short |
Supramolecular multilayer structures of wired redox enzyme electrodes |
| title_full |
Supramolecular multilayer structures of wired redox enzyme electrodes |
| title_fullStr |
Supramolecular multilayer structures of wired redox enzyme electrodes |
| title_full_unstemmed |
Supramolecular multilayer structures of wired redox enzyme electrodes |
| title_sort |
supramolecular multilayer structures of wired redox enzyme electrodes |
| publishDate |
2005 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v7_n8_p1800_Calvo http://hdl.handle.net/20.500.12110/paper_14639076_v7_n8_p1800_Calvo |
| work_keys_str_mv |
AT calvoernestojulio supramolecularmultilayerstructuresofwiredredoxenzymeelectrodes |
| _version_ |
1768543961278840832 |